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Q8DXM9

- GSHAB_STRA5

UniProt

Q8DXM9 - GSHAB_STRA5

Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.

    Catalytic activityi

    ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.UniRule annotation
    ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.UniRule annotation

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.By similarity

    Enzyme regulationi

    Inhibited by L-buthionine-S-sulfoximine (L-S-BSO).

    Kineticsi

    1. KM=22 mM for L-glutamate
    2. KM=156 µM for L-cysteine
    3. KM=8.2 mM for alpha-L-aminobutyrate
    4. KM=64 µM for ATP (in the reaction with gamma-GCS)
    5. KM=5.9 mM for gamma-L-glutamyl-L-cysteine
    6. KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate
    7. KM=6.3 mM for glycine
    8. KM=420 µM for ATP (in the reaction with GS)

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi696 – 6961Magnesium or manganese 1UniRule annotation
    Metal bindingi717 – 7171Magnesium or manganese 1UniRule annotation
    Metal bindingi717 – 7171Magnesium or manganese 2UniRule annotation
    Metal bindingi719 – 7191Magnesium or manganese 2UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi516 – 57459ATPUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. glutamate-cysteine ligase activity Source: UniProtKB-HAMAP
    3. glutathione synthase activity Source: UniProtKB-HAMAP
    4. magnesium ion binding Source: UniProtKB-HAMAP
    5. manganese ion binding Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Glutathione biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSAGA208435:GHVY-1917-MONOMER.
    BRENDAi6.3.2.3. 5917.
    SABIO-RKQ8DXM9.
    UniPathwayiUPA00142; UER00209.
    UPA00142; UER00210.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione biosynthesis bifunctional protein GshABUniRule annotation
    Alternative name(s):
    Gamma-GCS-GSUniRule annotation
    Short name:
    GCS-GSUniRule annotation
    Including the following 2 domains:
    Glutamate--cysteine ligaseUniRule annotation (EC:6.3.2.2UniRule annotation)
    Alternative name(s):
    Gamma-ECSUniRule annotation
    Short name:
    GCSUniRule annotation
    Gamma-glutamylcysteine synthetaseUniRule annotation
    Glutathione synthetaseUniRule annotation (EC:6.3.2.3UniRule annotation)
    Alternative name(s):
    GSH synthetaseUniRule annotation
    Short name:
    GSUniRule annotation
    Short name:
    GSH-SUniRule annotation
    Short name:
    GSHaseUniRule annotation
    Glutathione synthaseUniRule annotation
    Gene namesi
    Name:gshABUniRule annotation
    Synonyms:gshFUniRule annotation
    Ordered Locus Names:SAG1821
    OrganismiStreptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
    Taxonomic identifieri208435 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000821: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 750750Glutathione biosynthesis bifunctional protein GshABPRO_0000192559Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.Curated

    Protein-protein interaction databases

    STRINGi208435.SAG1821.

    Structurei

    Secondary structure

    1
    750
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 93
    Beta strandi19 – 3113
    Turni32 – 354
    Beta strandi44 – 463
    Turni49 – 513
    Beta strandi53 – 6715
    Beta strandi71 – 733
    Helixi74 – 9118
    Beta strandi96 – 983
    Beta strandi101 – 1033
    Turni109 – 1113
    Helixi120 – 13314
    Helixi136 – 1394
    Beta strandi143 – 1497
    Helixi151 – 16111
    Helixi166 – 19126
    Beta strandi199 – 2013
    Turni206 – 2083
    Beta strandi212 – 2143
    Beta strandi217 – 2215
    Helixi234 – 24310
    Turni246 – 2483
    Helixi253 – 2553
    Beta strandi259 – 2646
    Turni268 – 2747
    Beta strandi278 – 2814
    Helixi296 – 31116
    Helixi318 – 33417
    Helixi347 – 36115
    Helixi365 – 37915
    Helixi381 – 3833
    Helixi385 – 3928
    Helixi399 – 41315
    Helixi421 – 4233
    Helixi428 – 44013
    Beta strandi443 – 4475
    Beta strandi449 – 4513
    Beta strandi453 – 4586
    Beta strandi461 – 4666
    Turni467 – 4693
    Helixi477 – 4815
    Turni482 – 4843
    Helixi486 – 4949
    Turni507 – 5104
    Helixi511 – 5177
    Beta strandi518 – 5214
    Beta strandi523 – 5275
    Beta strandi532 – 5354
    Beta strandi537 – 5415
    Helixi545 – 55814
    Beta strandi560 – 5667
    Beta strandi570 – 5789
    Beta strandi581 – 5899
    Beta strandi592 – 5943
    Helixi601 – 6088
    Beta strandi614 – 6185
    Beta strandi621 – 6233
    Helixi629 – 6379
    Beta strandi651 – 6544
    Turni660 – 6634
    Beta strandi665 – 6684
    Turni670 – 6723
    Helixi675 – 68713
    Beta strandi694 – 7007
    Beta strandi702 – 7043
    Turni708 – 7114
    Beta strandi714 – 7218
    Helixi725 – 7284
    Beta strandi731 – 7333
    Helixi739 – 7468

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LN6X-ray2.95A1-750[»]
    ProteinModelPortaliQ8DXM9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini489 – 747259ATP-graspUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 333333Glutamate--cysteine ligaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.UniRule annotation
    Contains 1 ATP-grasp domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1181.
    HOGENOMiHOG000156471.
    KOiK01919.
    OMAiHVEYVKN.
    OrthoDBiEOG6BKJ7H.

    Family and domain databases

    Gene3Di3.30.470.20. 1 hit.
    HAMAPiMF_00782. Glut_biosynth.
    InterProiIPR011761. ATP-grasp.
    IPR013816. ATP_grasp_subdomain_2.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    [Graphical view]
    PfamiPF04262. Glu_cys_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8DXM9-1 [UniParc]FASTAAdd to Basket

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    MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN    50
    YHPYIQTDYS EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP 100
    LSMPPKVREE DIQIAQLEDA FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG 150
    QELLTSLFEL SQADNAIDFQ NQLYMKLSQN FLRYRWLLTY LYGASPVAEE 200
    DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND LENAVKSGQL 250
    IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD 300
    TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL 350
    VDAMQSVIQH FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET 400
    FGQRQGQIYH DYAWEAPYAL KGYETMELST QLLLFDVIQK GVNFEVLDEQ 450
    DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL AMANKVVTKK ILDEKHFPTP 500
    FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK TSANLASYEK 550
    AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT 600
    ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT 650
    KIELRRNSNI STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP 700
    NATQAYSKDK KNATCIELNF NPLMYMHTYC QEGPGQSITP RILAKLFPEL 750
    Length:750
    Mass (Da):85,603
    Last modified:March 1, 2003 - v1
    Checksum:i97829C2C5B44174A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009948 Genomic DNA. Translation: AAN00684.1.
    RefSeqiNP_688811.1. NC_004116.1.

    Genome annotation databases

    EnsemblBacteriaiAAN00684; AAN00684; SAG1821.
    GeneIDi1014630.
    KEGGisag:SAG1821.
    PATRICi19630489. VBIStrAga72745_1829.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009948 Genomic DNA. Translation: AAN00684.1 .
    RefSeqi NP_688811.1. NC_004116.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LN6 X-ray 2.95 A 1-750 [» ]
    ProteinModelPortali Q8DXM9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208435.SAG1821.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN00684 ; AAN00684 ; SAG1821 .
    GeneIDi 1014630.
    KEGGi sag:SAG1821.
    PATRICi 19630489. VBIStrAga72745_1829.

    Phylogenomic databases

    eggNOGi COG1181.
    HOGENOMi HOG000156471.
    KOi K01919.
    OMAi HVEYVKN.
    OrthoDBi EOG6BKJ7H.

    Enzyme and pathway databases

    UniPathwayi UPA00142 ; UER00209 .
    UPA00142 ; UER00210 .
    BioCyci SAGA208435:GHVY-1917-MONOMER.
    BRENDAi 6.3.2.3. 5917.
    SABIO-RK Q8DXM9.

    Family and domain databases

    Gene3Di 3.30.470.20. 1 hit.
    HAMAPi MF_00782. Glut_biosynth.
    InterProi IPR011761. ATP-grasp.
    IPR013816. ATP_grasp_subdomain_2.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    [Graphical view ]
    Pfami PF04262. Glu_cys_ligase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01435. glu_cys_lig_rel. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-611 / 2603 V/R.
    2. "Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities."
      Janowiak B.E., Griffith O.W.
      J. Biol. Chem. 280:11829-11839(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: ATCC BAA-611 / 2603 V/R.

    Entry informationi

    Entry nameiGSHAB_STRA5
    AccessioniPrimary (citable) accession number: Q8DXM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3